Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
oligomer
x * 20000, SDS-PAGE
?
x * 24484, isozyme PPa1, DNA sequence calculation, x * 24576, isozyme PPa4, DNA sequence calculation
?
x * 32000, calculated from amino acid sequence
?
-
x * 20000, calculated from amino acid sequence
?
-
x * 20000, calculated from amino acid sequence
-
?
x * 33500, about, sequence calculation
?
x * 32000, calculated from amino acid sequence
?
x * 32000, calculated from amino acid sequence
?
-
x * 24400, p26.1a, SDS-PAGE, x * 26500, p26.1b, SDS-PAGE
?
x * 24500, recombinant enzyme, SDS-PAGE, x * 20833, amino acid sequence calculation
?
-
x * 24500, recombinant enzyme, SDS-PAGE, x * 20833, amino acid sequence calculation
-
?
DQ978330
x * 33000, recombinant enzyme, SDS-PAGE
?
-
x * 34000, SDS-PAGE
-
?
-
x * 19365, calculated
?
-
x * 19435, calculated
?
-
x * 19435, calculated
-
?
-
x * 32000, calculated from amino acid sequence
?
x * 20850, calculated from amino acid sequence
?
-
x * 45000, His-tagged enzyme, SDS-PAGE
?
-
x * 47900, calculated from amino acid sequence
dimer
-
2 * 34000, dimer when inactive
dimer
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview
dimer
-
2 * 33000, SDS-PAGE
dimer
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview. The isolated regulatory part (residues 66-306) of Clostridium perfringens CBS-PPase, comprised of two CBS domains and one DRTGG domain, dimerizes by forming CBS1-CBS1', CBS2-CBS2', and DRTGG-DRTGG' contacts. Two interacting pairs of CBS domains (Bateman modules) form a disk-like structure (CBS module), characteristic of CBS domain-containing proteins
dimer
-
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview. The isolated regulatory part (residues 66-306) of Clostridium perfringens CBS-PPase, comprised of two CBS domains and one DRTGG domain, dimerizes by forming CBS1-CBS1', CBS2-CBS2', and DRTGG-DRTGG' contacts. Two interacting pairs of CBS domains (Bateman modules) form a disk-like structure (CBS module), characteristic of CBS domain-containing proteins
-
dimer
-
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview. The isolated regulatory part (residues 66-306) of Clostridium perfringens CBS-PPase, comprised of two CBS domains and one DRTGG domain, dimerizes by forming CBS1-CBS1', CBS2-CBS2', and DRTGG-DRTGG' contacts. Two interacting pairs of CBS domains (Bateman modules) form a disk-like structure (CBS module), characteristic of CBS domain-containing proteins
-
dimer
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview
dimer
-
an active dimer can be obtained using 20% isopropanol from the native hexamer
dimer
-
2 * 70000, SDS-PAGE
dimer
-
2 * 20000, SDS-PAGE
dimer
-
2 * 25000, SDS-PAGE
dimer
-
the enzyme CBS-PPase contains cystathionine beta-synthase domains
dimer
-
2 * 35000, SDS-PAGE
dimer
2 * 45000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 32000, SDS-PAGE
dimer
-
2 * 32042, amino acid sequence
dimer
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview
dimer
the enzyme structure consists of two domains, comprising residues 1-191 and 198-311, respectively, with the active site located between them, overview
dimer
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview
dimer
2 * 33407, mass spectrometry
dimer
1 x * 27000 + 1 * 57000, recombinant mutant I259V, native PAGE in absence of Mn2+, 1 * 32000 + 1 x 62000, recombinant wild-type enzyme, native PAGE in absence of Mn2+
dimer
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview
dimer
-
1 x * 27000 + 1 * 57000, recombinant mutant I259V, native PAGE in absence of Mn2+, 1 * 32000 + 1 x 62000, recombinant wild-type enzyme, native PAGE in absence of Mn2+
-
dimer
-
2 * 33407, mass spectrometry
-
dimer
-
each subunit of dimeric canonical Family II PPases is formed by two domains connected by a flexible linker, with the active site located between the domains. Canonical Family II PPases structures, domain structures, overview
-
dimer
-
2 * 33000, SDS-PAGE
dimer
-
TgPPase forms dimers in solution and in the crystal. Structure comparisons of the enzyme from Plasmodium falciparum (PfPPase) and Toxoplasma gondii (TgPPase), overview
dimer
-
the homodimer contains several transmembrane segments, the conserved transmembrane segment 5 at the N-terminal side near the putative substrate binding loop contains the GYG motif which is important in maintaining structure and function of the enzyme, overview
hexamer
6 * 20000, SDS-PAGE
hexamer
-
6 * 20000, sedimentation equilibrium
hexamer
-
6 * 20000, (alpha3)2
hexamer
-
6 * 20000, homohexameric, 175 amino acid residues per subunit, wild type enzyme
hexamer
-
composed of two trimers
hexamer
-
native form, composed of two trimers
hexamer
-
dimer of active trimers
hexamer
-
two trimers, preparation of wild-type trimers by incubation of enzyme in 0.1 M MES-NaOH, pH 5.3, for 20 h at 25°C, and of the mutant K112Q in 0.1 M Na-citrate buffer, pH 4.5, for 20 h at 25°C
hexamer
-
6 * 19100, SDS-PAGE
hexamer
-
6 * 19272, amino acid sequence calculation, structure-based phylogenetic tree of diphosphatases, overview
hexamer
6 * 20675, recombinant His-tagged enzyme, mass spectrometry
hexamer
-
6 * 19100, SDS-PAGE
-
hexamer
-
dimeric trimer, crystal structure
hexamer
6 * 19 187, mass spectrometry
hexamer
6 * 22000, SDS-PAGE
homodimer
-
-
homodimer
2 * 35000, SDS-PAGE
homodimer
-
2 * 35000, SDS-PAGE
-
homodimer
2 * 22000, SDS-PAGE
homodimer
2 * 21740, calculated from amino acid sequence
homodimer
-
2 * 22000, SDS-PAGE
-
homodimer
-
2 * 21740, calculated from amino acid sequence
-
homodimer
2 * 34000, SDS-PAGE
homodimer
-
2 * 34000, SDS-PAGE
-
homohexamer
6 * 25000, crecombinant detagged enzyme, SDS-PAGE
homohexamer
6 * 27000, SDS-PAGE
homohexamer
6 * 24500, dimer of trimers, recombinant detagged enzyme, SDS-PAGE
homotetramer
4 * 20000, SDS-PAGE
homotetramer
4 * 18600, calculated from amino acid sequence
monomer
1 * 24000, isozyme sPPase-II, SDS-PAGE, 1 * 24350, isozyme sPPase-II, mass spectrometry
monomer
1 * 30000, isozyme sPPase-I, SDS-PAGE, 1 * 29850, isozyme sPPase-I, mass spectrometry
monomer
-
1 * 60000, SDS-PAGE
monomer
-
1 * 55000, SDS-PAGE
monomer
1 * 26000, SDS-PAGE
monomer
-
1 * 26000, SDS-PAGE
-
tetramer
-
4 * 20000, SDS-PAGE
tetramer
4 * 33500, SDS-PAGE, 4 * 33494, sequence calculation
tetramer
-
4 * 33500, SDS-PAGE, 4 * 33494, sequence calculation
-
tetramer
-
4 * 32500, SDS-PAGE
tetramer
-
4 * 25000, gel filtration, dimeric form also active
tetramer
-
4 * 25000, gel filtration, dimeric form also active
-
tetramer
-
4 * 21000, SDS-PAGE
tetramer
-
4 * 17000-18000, SDS-PAGE
tetramer
-
4 * 17000, SDS-PAGE, 4 * 19365, calculated
tetramer
4 * 19365, calculated from sequence
tetramer
-
4 * 21000, SDS-PAGE
-
tetramer
-
4 * 19365, calculated from sequence
-
trimer
-
3 * 34000, trimer when active
trimer
-
dissociated variant, SDS-PAGE
additional information
circular dichroism spectrum, secondary structure of isozymes, overview
additional information
topology and conformation of the PPA1 subunits, comparison to the enzyme from Medicago truncatula. The N-terminal peptide of immature AtPPA1 is mostly disordered
additional information
-
topology and conformation of the PPA1 subunits, comparison to the enzyme from Medicago truncatula. The N-terminal peptide of immature AtPPA1 is mostly disordered
additional information
-
B-cell epitope mapping of the recombinant enzyme, epitopes are spread across the whole enzyme molecule
additional information
structure modeling and structure-function analysis, overview. BT2127 conserves the His23-Lys79 diad, and in both the cap-open and -closed conformations, the Asp13 side chain is in the same conformation, engaged in a hydrogen bond with linker residue Ser15
additional information
-
structure modeling and structure-function analysis, overview. BT2127 conserves the His23-Lys79 diad, and in both the cap-open and -closed conformations, the Asp13 side chain is in the same conformation, engaged in a hydrogen bond with linker residue Ser15
additional information
-
structure modeling and structure-function analysis, overview. BT2127 conserves the His23-Lys79 diad, and in both the cap-open and -closed conformations, the Asp13 side chain is in the same conformation, engaged in a hydrogen bond with linker residue Ser15
-
additional information
peptide mass fingerprint analysis of isozyme sPPase-I
additional information
peptide mass fingerprint analysis of isozyme sPPase-I
additional information
-
peptide mass fingerprint analysis of isozyme sPPase-I
additional information
peptide mass fingerprint analysis of isozyme sPPase-II
additional information
peptide mass fingerprint analysis of isozyme sPPase-II
additional information
-
peptide mass fingerprint analysis of isozyme sPPase-II
additional information
-
trimers, dimers and monomers can be obtained using isopropanol and weak acid, all forms are catalytically active with lowest activity for the monomer
additional information
ThPP1 gene exhibits a typical structural characteristic of PPase family. ThPP1 protein is a hydrolase with the sites of metal binding protein, but having a tight single domain without the transmembrane structure
additional information
-
ThPP1 gene exhibits a typical structural characteristic of PPase family. ThPP1 protein is a hydrolase with the sites of metal binding protein, but having a tight single domain without the transmembrane structure
additional information
three-dimensional homology modeling suggests HvPPA to have an OB fold consisting of a central beta-barrel structure and alpha-helices associated in a beta1-8-alpha1-beta9-alpha2 topology and to homo-oligomerize into a trimer and/or dimer of trimers
additional information
-
three-dimensional homology modeling suggests HvPPA to have an OB fold consisting of a central beta-barrel structure and alpha-helices associated in a beta1-8-alpha1-beta9-alpha2 topology and to homo-oligomerize into a trimer and/or dimer of trimers
additional information
structure analysis, PPase comprises three alpha-helices and nine beta-strands and folds as a barrel structure, it forms a hexamer in both the solution and crystal states, and each monomer has its own PPi-binding site
additional information
-
structure analysis, PPase comprises three alpha-helices and nine beta-strands and folds as a barrel structure, it forms a hexamer in both the solution and crystal states, and each monomer has its own PPi-binding site
additional information
topology and conformation of the PPA1 subunits, comparison to the enzyme from Arabidospis thaliana
additional information
-
topology and conformation of the PPA1 subunits, comparison to the enzyme from Arabidospis thaliana
additional information
structure comparison of family I enzymes, overview
additional information
-
structure comparison of family I enzymes, overview
additional information
-
structure comparison of family I enzymes, overview
-
additional information
enzyme PfPPase exists predominantly as a dimer in solution with a minor tetrameric peak. PfPPase low complexity asparagine-rich N-terminal region mediates its dimerization. Structure comparisons of the enzyme from Plasmodium falciparum (PfPPase) and Toxoplasma gondii (TgPPase), overview
additional information
-
enzyme PfPPase exists predominantly as a dimer in solution with a minor tetrameric peak. PfPPase low complexity asparagine-rich N-terminal region mediates its dimerization. Structure comparisons of the enzyme from Plasmodium falciparum (PfPPase) and Toxoplasma gondii (TgPPase), overview
additional information
-
structural basis for the high thermostability
additional information
the free N- and C-terminal domains do not interact productively, when mixed together, the interdomain region has the function of a mechanical hinge, structure modelling
additional information
-
the free N- and C-terminal domains do not interact productively, when mixed together, the interdomain region has the function of a mechanical hinge, structure modelling
additional information
the hinge region plays an important role in opening and closing of the active site between the N- and C-terminal domains of PPase. Family II PPases are dimer under physiological conditions with Mn2+ present, and may dissociate into monomers at low enzyme concentration in the absence of Mn2+
additional information
-
the hinge region plays an important role in opening and closing of the active site between the N- and C-terminal domains of PPase. Family II PPases are dimer under physiological conditions with Mn2+ present, and may dissociate into monomers at low enzyme concentration in the absence of Mn2+
additional information
-
the hinge region plays an important role in opening and closing of the active site between the N- and C-terminal domains of PPase. Family II PPases are dimer under physiological conditions with Mn2+ present, and may dissociate into monomers at low enzyme concentration in the absence of Mn2+
-
additional information
-
the free N- and C-terminal domains do not interact productively, when mixed together, the interdomain region has the function of a mechanical hinge, structure modelling
-
additional information
-
analysis of amino acid composition and comparison with Escherichia coli, saccharomyces cerevisiae and Bacillus sp. enzymes
additional information
-
analysis of amino acid composition and comparison with Escherichia coli, saccharomyces cerevisiae and Bacillus sp. enzymes
-